eF-site ID 1okv-C
PDB Code 1okv
Chain C

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Title Cyclin A binding groove inhibitor H-Arg-Arg-Leu-Ile-Phe-NH2
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound CELL DIVISION PROTEIN KINASE 2
Source Homo sapiens (Human) (1OKV)
Sequence C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHL
Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.1.37), CYCLIN A2, H-ARG-ARG-LEU-ILE-PHE-NH2


Functional site

1) chain C
residue 247
type
ligand
sequence D
description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2
source : AC2

2) chain C
residue 127
type ACT_SITE
ligand
sequence D
description Proton acceptor.
source Swiss-Prot : SWS_FT_FI6

3) chain C
residue 132
type METAL
ligand
sequence N
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI7

4) chain C
residue 145
type METAL
ligand
sequence D
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI7

5) chain C
residue 33
type BINDING
ligand
sequence K
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

6) chain C
residue 86
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

7) chain C
residue 145
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

8) chain C
residue 9
type SITE
ligand
sequence K
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

9) chain C
residue 88-89
type SITE
ligand
sequence KK
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

10) chain C
residue 166
type SITE
ligand
sequence L
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

11) chain C
residue 10-18
type NP_BIND
ligand
sequence IGEGTYGVV
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

12) chain C
residue 81-83
type NP_BIND
ligand
sequence EFL
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

13) chain C
residue 129-132
type NP_BIND
ligand
sequence KPQN
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

14) chain C
residue 131
type catalytic
ligand
sequence Q
description Annotated By Reference To The Literature 1ir3
source CSA : CSA2

15) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA2

16) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA4

17) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA4

18) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

19) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

20) chain C
residue 165
type catalytic
ligand
sequence T
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

21) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8

22) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8

23) chain C
residue 132
type catalytic
ligand
sequence N
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8


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